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Max Ferdinand PerutzChemist, Nobel Prize in Chemistry, 1962 (shared with D. Kendrew)
Date of Birth: 19.05.1914
Country:  Great Britain |
Content:
- Max Perutz: Nobel Prize-Winning Biochemist
- Cambridge University and X-ray Crystallography
- Wartime Interruption
- Secret Allied Project
- Post-War Research and Molecular Biology
- Isomorphic Replacement and Protein Structure
- Three-Dimensional Model of Hemoglobin
- Nobel Prize and Later Career
- Legacy
Max Perutz: Nobel Prize-Winning Biochemist
Early Life and EducationMax Ferdinand Perutz was born in Vienna, Austria, in 1914, to wealthy textile manufacturers. Despite his parents' desire for him to pursue law, Perutz developed a passion for chemistry. In 1932, he enrolled in the University of Vienna to study inorganic chemistry but soon switched to organic chemistry.
Cambridge University and X-ray Crystallography
Intrigued by the research in X-ray crystallography at the University of Cambridge, Perutz moved to England in 1936. He worked with physicist John Desmond Bernal at the Cavendish Laboratory, where he изучил method of X-ray diffraction. In 1937, he initiated research on hemoglobin, the oxygen-carrying protein in blood.
Wartime Interruption
The outbreak of World War II paused Perutz's research. In 1938, he lost financial support from his parents due to Nazi annexation of Austria. Thanks to the intervention of physicist William Lawrence Bragg, Perutz obtained a Rockefeller Foundation grant. He remained at Cambridge as Bragg's assistant, earning his doctorate in 1940.
Secret Allied Project
Interned in Canada as an enemy subject in 1941, Perutz became fascinated by glacial properties. He joined a secret Allied project under Lord L. Mountbatten, exploring the use of ice fields as airfields.
Post-War Research and Molecular Biology
After the war, Perutz returned to studying hemoglobin with a post-doctoral fellowship from the Imperial Chemical Industries. In 1947, he became head of the newly formed Molecular Biology Research Group at the University of Cambridge. Initially working with John Kendrew, the group grew to include the likes of Francis Crick, James Watson, and Frederick Sanger.
Isomorphic Replacement and Protein Structure
Perutz's breakthrough came in 1953 with the development of the isomorphous replacement method. By introducing heavy metal atoms into protein crystals, he obtained different X-ray diffraction patterns. Comparing these patterns revealed the positions of specific atoms, providing crucial information about the crystal structure.
Three-Dimensional Model of Hemoglobin
By 1956, Perutz had obtained X-ray photographs of hemoglobin molecules with heavy atoms located at different sites. By 1957, he could resolve objects separated by 6 Å. Over the next three years, he collected thousands of photographic plates, processed the data with computers, and finally proposed a model for the three-dimensional structure of hemoglobin in 1960.
Nobel Prize and Later Career
Perutz's findings were published in "Nature" in February 1960. In 1962, he and Kendrew were awarded the Nobel Prize in Chemistry "for their studies of the structures of globular proteins." Perutz continued to study hemoglobin after retiring as the head of the Molecular Biology Laboratory in 1979. He served as a British Ministry of Defense consultant, Chairman of the European Molecular Biology Organization, and Professor of Physiology at the Royal Institution.
Legacy
Perutz, an avid skier and mountaineer, once described his interest in glaciers as "mostly an excuse to work in the mountains." Despite his shy demeanor, he was known among his colleagues as a highly tenacious researcher. His pioneering work in X-ray crystallography and determination of protein structure transformed the understanding of biological molecules.
